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Caldesmon Is Necessary for Maintaining the Actin and Intermediate Filaments in Cultured Bladder Smooth Muscle Cells by Maoxian Deng; Sunish Mohanan; Erzsebet Polyak; Samuel Chacko is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

## Abstract Caldesmon (CaD), a component of microfilaments in all cells and thin filaments in smooth muscle cells, is known to bind to actin, tropomyosin, calmodulin, and myosin and to inhibit actin‐activated ATP hydrolysis by smooth muscle myosin. Thus, it is believed to regulate smooth muscle contraction, cell motility and the cytoskeletal structure. Using bladder smooth muscle cell cultures and RNA interference (RNAi) technique, we show that the organization of actin into microfilaments in the cytoskeleton is diminished by siRNA‐mediated CaD silencing. CaD silencing significantly decreased the amount of polymerized actin (F‐actin), but the expression of actin was not altered. Additionally, we find that CaD is associated with 10 nm intermediate‐sized filaments (IF) and in vitro binding assay reveals that it binds to vimentin and desmin proteins. Assembly of vimentin and desmin into IF is also affected by CaD silencing, although their expression is not significantly altered when CaD is silenced. Electronmicroscopic analyses of the siRNA‐treated cells showed the presence of myosin filaments and a few surrounding actin filaments, but the distribution of microfilament bundles was spa

Author

Maoxian Deng; Sunish Mohanan; Erzsebet Polyak; Samuel Chacko

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0886-1544)

Published

2007

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)